Premium
Association and colocalization of G protein α subunits and Purkinje cell protein 2 (Pcp2) in mammalian cerebellum
Author(s) -
Redd Kacy J.,
Oberdick John,
McCoy John,
Denker Bradley M.,
Luo Yuan
Publication year - 2002
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.10460
Subject(s) - colocalization , cerebellum , neuroscience , purkinje cell , cell type , biology , psychology , microbiology and biotechnology , cell , biochemistry
Previously, we have demonstrated a novel interaction between Gα o protein and Purkinje cell protein‐2 (Pcp2, also known as L7) in vitro and in transfected cells (Luo and Denker [1999] J. Biol. Chem. 274:10685–10688). Pcp2 is uniquely expressed in cerebellar Purkinje cells and in retinal bipolar neurons, and it may function as a cell‐type specific modulator for G protein‐mediated cell signaling. This interaction has been further evaluated in the present studies. Coimmunoprecipitation experiments reveal that Pcp2 associates with Gα o in vivo in mouse cerebellum and eye extract. Pcp2 also associate with Gα i2 in the cerebellum. No detectable associations of Pcp2 with Gα z and Gα q subunits are observed. The association of Gα o and Pcp2 is detected at postnatal day 1 (P1), and the association remains stable from day 3 (P3) until adulthood. Further, immunofluorescent double labeling and confocal microscopy suggest that Pcp2 and Gα o are colocalized in the distal processes of cerebellar Purkinje cells including axonal endings and dendritic spines. Taken together, these findings indicate colocalization and association of Gα o and Pcp2 in cerebellum and suggest a functional role in regions of synaptic activity. © 2002 Wiley‐Liss, Inc.